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Link to original content: https://pubmed.ncbi.nlm.nih.gov/11287959
CaT1 manifests the pore properties of the calcium-release-activated calcium channel - PubMed Skip to main page content
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. 2001 Apr 5;410(6829):705-9.
doi: 10.1038/35070596.

CaT1 manifests the pore properties of the calcium-release-activated calcium channel

L Yue  1 , J B Peng, M A Hediger, D E Clapham
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CaT1 manifests the pore properties of the calcium-release-activated calcium channel

L Yue et al. Nature. .

Abstract

The calcium-release-activated Ca2+channel, ICRAC, is a highly Ca2+-selective ion channel that is activated on depletion of either intracellular Ca2+ levels or intracellular Ca2+ stores. The unique gating of ICRAC has made it a favourite target of investigation for new signal transduction mechanisms; however, without molecular identification of the channel protein, such studies have been inconclusive. Here we show that the protein CaT1 (ref. 4), which has six membrane-spanning domains, exhibits the unique biophysical properties of ICRAC when expressed in mammalian cells. Like ICRAC, expressed CaT1 protein is Ca2+ selective, activated by a reduction in intracellular Ca2+ concentration, and inactivated by higher intracellular concentrations of Ca2+. The channel is indistinguishable from ICRAC in the following features: sequence of selectivity to divalent cations; an anomalous mole fraction effect; whole-cell current kinetics; block by lanthanum; loss of selectivity in the absence of divalent cations; and single-channel conductance to Na+ in divalent-ion-free conditions. CaT1 is activated by both passive and active depletion of calcium stores. We propose that CaT1 comprises all or part of the ICRAC pore.

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